Saito H, Takase M, Tamura Y, Shimamura S, Tomita M
Nutritional Science Laboratory, Morinaga Milk Industry Co., Ltd., Kanagawa, Japan.
Adv Exp Med Biol. 1994;357:219-26. doi: 10.1007/978-1-4615-2548-6_21.
In order to apply functionally active lactoferrin (Lf) to food products, the effect of pH on the heat stability of Lf was studied. Lf was easily denatured to an insoluble state by heat treatment under neutral or alkaline conditions, above pH 6. In contrast, it remained soluble after heat treatment under acidic conditions at pH 2 to 5, and the HPLC pattern of Lf heat-treated at pH 4 at 100 degrees C for 5 min was the same as that of native Lf. Lf was found to be very thermostable at pH 4, and could be pasteurized or sterilized without any significant loss of its physicochemical properties. Lf was hydrolyzed by heat treatment at pH 2 to 3 at above 100 degrees C, and its iron binding capacity and antigenicity were lost. But the antibacterial activity of the hydrolysate was found to be much stronger than that of native Lf. The antibacterial component of Lf hydrolysate produced by heat treatment at acidic pH was verified to be a peptide including the sequence of residues 1-54 from the N-terminal end of the bovine Lf molecule.
为了将具有功能活性的乳铁蛋白(Lf)应用于食品,研究了pH对Lf热稳定性的影响。在pH 6以上的中性或碱性条件下,Lf通过热处理容易变性为不溶状态。相比之下,在pH 2至5的酸性条件下热处理后它仍保持可溶,并且在100℃下于pH 4热处理5分钟的Lf的HPLC图谱与天然Lf的图谱相同。发现Lf在pH 4时非常耐热,并且可以进行巴氏杀菌或灭菌而其理化性质没有任何显著损失。在高于100℃的pH 2至3条件下通过热处理Lf会被水解,并且其铁结合能力和抗原性丧失。但是发现水解产物的抗菌活性比天然Lf的抗菌活性强得多。经证实,在酸性pH下通过热处理产生的Lf水解产物的抗菌成分是一种肽,其包含来自牛Lf分子N末端的1-54位残基的序列。